Accumulation of viruslike particles in a yeast mutant lacking a mitochondrial pore protein

Mol Cell Biol. 1989 Mar;9(3):1100-8. doi: 10.1128/mcb.9.3.1100-1108.1989.


The lack of mitochondrial porin is not lethal in Saccharomyces cerevisiae, but it impairs some respiratory functions and, therefore, growth on nonfermentable carbon sources such as glycerol. However, after a lag phase porinless mutant cells adapt to growth on glycerol, accumulating large amounts of an 86-kilodalton (kDa) protein (M. Dihanich, K. Suda, and G. Schatz, EMBO J. 6:723-728, 1987) and of a 5-kilobase RNA. Immunogold labeling localized the 86 kDa-protein exclusively to the cytosol fraction, although most of it cosedimented with the microsome fraction in earlier cell fractionations. This discrepancy was resolved when the 86-kDa protein was identified as the major coat protein in viruslike particles (VLPs) which is encoded by a double-stranded RNA (L-A RNA). Elimination of VLPs in the original porinless strain by introduction of the mak10 or the mak3 mutation increased the respiratory defect and prolonged its lag phase on nonfermentable carbon sources. The fact that the simultaneous loss of VLPs and respiratory functions are the introduction of mak10 or mak3 occurred even in some porin-containing wild-type strains suggests that there is a link between VLP and mitochondrial functions.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Capsid / metabolism
  • DNA Probes
  • DNA, Fungal / genetics
  • Genes, Fungal
  • Inclusion Bodies, Viral / ultrastructure*
  • Membrane Proteins / genetics*
  • Membrane Proteins / metabolism
  • Microscopy, Electron
  • Mitochondria / metabolism
  • Molecular Sequence Data
  • Mutation
  • Porins*
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae / ultrastructure*
  • Voltage-Dependent Anion Channels


  • DNA Probes
  • DNA, Fungal
  • Membrane Proteins
  • Porins
  • Voltage-Dependent Anion Channels